[Untitled]

To study the transfer of oxidized phospholipids from cell membranes to high-density lipoproteins (HDL), human Cu2+-oxidized erythrocyte membranes were incubated with HDL3 subfraction for 17 h at 37°C followed by isolation of the supernatant, precipitation from it of HDL3, and determination of lipid peroxide products (LPP) in them. The incubation increased the content of lipid hydroperoxides in HDL3 significantly (by 32 and 40% calculated per ml of sample or mg of protein) and of malondialdehyde (by 27 and 34%, respectively) compared to control (incubation of HDL3 alone). The content of conjugated dienes did not change significantly. Fluorescence analyses of isolated HDL3 particles showed that the content of fluorescent products (λex = 365 nm, λem = 430 nm) in them was 2.5 times higher than in control, and the number of binding sites for the 1-anilinonaphthalene-8-sulfonic acid probe decreased by 22%. This also confirms accumulation of LPP in the lipoprotein subfraction. It seems likely that an increase in LPP (at least hydroperoxides) in HDL3 after their incubation with oxidized membranes occurs via transport of phospholipids containing LPP from erythrocyte membranes to lipoproteins. The data on the ability of HDL3 to accept LPP from erythrocyte membranes in vitro suggest that HDL3 may have a protective action on cell membranes undergoing oxidation in vivo as well.